P11393 (PHEB_PORCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
B-phycoerythrin beta chain

Gene names

Name:

cpeB

Encoded on

Plastid; Chloroplast

Organism

Porphyridium cruentum (Red alga)

Taxonomic identifier

35688 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Rhodophyta › Bangiophyceae › Porphyridiales › Porphyridiaceae › Porphyridium

Protein attributes

Sequence length	177 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.
Subunit structure	Heteropolymer of 6 alpha, 6 beta and one gamma chain By similarity.
Subcellular location	Plastid › chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side By similarity. Note: Forms the periphery of the phycobilisome rod By similarity.
Post-translational modification	Contains two covalently linked phycoerythrobilin chromophores and one covalently linked phycourobilin chromophore.
Sequence similarities	Belongs to the phycobiliprotein family.

Ontologies

Keywords
Biological process	Electron transport Photosynthesis Transport
Cellular component	Chloroplast Membrane Phycobilisome Plastid Thylakoid
Ligand	Bile pigment Chromophore
PTM	Methylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis Inferred from electronic annotation. Source: UniProtKB-KW protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell phycobilisome Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 177

177

B-phycoerythrin beta chain

PRO_0000199194

Sites

Binding site

50

1

Phycourobilin chromophore (covalent; via 2 links)

Binding site

61

1

Phycourobilin chromophore (covalent; via 2 links)

Binding site

82

1

Phycoerythrobilin chromophore 1 (covalent; via 1 link)

Binding site

158

1

Phycoerythrobilin chromophore 2 (covalent; via 1 link)

Amino acid modifications

Modified residue

72

1

N4-methylasparagine Ref.1

Experimental info

Sequence conflict

167

1

S → Q AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

177

Helix Strand Turn

Details...

Helix

4 – 14

11

Helix

21 – 32

12

Helix

34 – 45

12

Helix

48 – 62

15

Helix

64 – 67

4

Helix

76 – 99

24

Helix

103 – 108

6

Turn

109 – 112

4

Helix

113 – 120

8

Helix

124 – 142

19

Helix

159 – 176

18

Sequences

	Sequence		Length	Mass (Da)
	P11393 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 168E71372A29CD89	FASTA	177	18,554
	10 20 30 40 50 60 MLDAFSRVVV NSDAKAAYVG GSDLQALKSF IADGNKRLDA VNSIVSNASC MVSDAVSGMI 70 80 90 100 110 120 CENPGLISPG GNCYTNRRMA ACLRDGEIIL RYVSYALLAG DASVLEDRCL NGLKETYIAL 130 140 150 160 170 GVPTNSSIRA VSIMKAQAVA FITNTATERK MSFAAGDCTS LASEVASYFD RVGAAIS

References

[1]	"The complete amino-acid sequence of the alpha and beta subunits of B-phycoerythrin from the rhodophytan alga Porphyridium cruentum." Sidler W., Kumpf B., Suter F., Klotz A.V., Glazer A.N., Zuber H. Biol. Chem. Hoppe-Seyler 370:115-124(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, METHYLATION AT ASN-72.
[2]	"Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Amino acid sequence studies." Lundell D.J., Glazer A.N., DeLange R.J., Brown D.M. J. Biol. Chem. 259:5472-5480(1984) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 38-77; 79-84 AND 151-171, CHROMOPHORE ATTACHMENT SITES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

S02818.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3V57	X-ray	1.70	B/D	1-177	[»]
3V58	X-ray	1.85	B/D	1-177	[»]

ProteinModelPortal

P11393.

SMR

P11393. Positions 1-177.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.490.20. 1 hit.

InterPro

IPR009050. Globin-like.
IPR012128. Phycobilisome_asu/bsu.
[Graphical view]

Pfam

PF00502. Phycobilisome. 1 hit.
[Graphical view]

PIRSF

PIRSF000081. Phycocyanin. 1 hit.

SUPFAM

SSF46458. Globin_like. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PHEB_PORCR

Accession

Primary (citable) accession number: P11393

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)